Calcineurin, a Calcium/Calmodulin-dependent Protein Phosphatase, Is Involved in Movement, Fertility, Egg Laying, and Growth in<i>Caenorhabditis elegans</i>

Jaya Bandyopadhyay(Gwangju Institute of Science and Technology), Jiyeon Lee(Gwangju Institute of Science and Technology), Jungsoo Lee(Gwangju Institute of Science and Technology), Jin Il Lee(Gwangju Institute of Science and Technology), Jae-Ran Yu(Konkuk University), Changhoon Jee(Gwangju Institute of Science and Technology), Jeong Hoon Cho(Gwangju Institute of Science and Technology), Sunki Jung(Gwangju Institute of Science and Technology), Myon‐Hee Lee(Yonsei University), Sonia Zannoni(Rutgers, The State University of New Jersey), Andrew Singson(Rutgers, The State University of New Jersey), Do Han Kim(Gwangju Institute of Science and Technology), Hyeon‐Sook Koo(Yonsei University), Joohong Ahnn(Gwangju Institute of Science and Technology)
Molecular Biology of the Cell
September 1, 2002
Cited by 119

Abstract

Calcineurin is a Ca(2+)-calmodulin-dependent serine/threonine protein phosphatase that has been implicated in various signaling pathways. Here we report the identification and characterization of calcineurin genes in Caenorhabditis elegans (cna-1 and cnb-1), which share high homology with Drosophila and mammalian calcineurin genes. C. elegans calcineurin binds calcium and functions as a heterodimeric protein phosphatase establishing its biochemical conservation in the nematode. Calcineurin is expressed in hypodermal seam cells, body-wall muscle, vulva muscle, neuronal cells, and in sperm and the spermatheca. cnb-1 mutants showed pleiotropic defects including lethargic movement and delayed egg-laying. Interestingly, these characteristic defects resembled phenotypes observed in gain-of-function mutants of unc-43/Ca(2+)-calmodulin-dependent protein kinase II (CaMKII) and goa-1/G(o)-protein alpha-subunit. Double mutants of cnb-1 and unc-43(gf) displayed an apparent synergistic severity of movement and egg-laying defects, suggesting that calcineurin may have an antagonistic role in CaMKII-regulated phosphorylation signaling pathways in C. elegans.


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